Elementary theory of angular momentum by M.E. (Morris Edgar) Rose

By M.E. (Morris Edgar) Rose

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Biochim. et Biophys. Acta 25, 100 (1957). , and Wustrow, H. J . Biochim. et Biophys. Acta 25, 110 (1957). , and Weber, H. H. Biochim. et Biophys. Acta 11, 160 (1953). Attempts toward a Formulation of Biological Use of Energy in Terms of Chemical Potentials FRITZ LIPMANN The Rockefeller Institute, New York, New York Chemical and biological definitions are becoming more and more confluent. In this situation, terminologies occasionally need a mutual adjustment for which some common sense has to be used.

17. 18. 19. , and Connelly, C. M. Nature 179, 1235 ( 1 9 5 7 ) . , Janke, J . , Davies, R . E . , and Krebs, Η. A. Nature 174, 1081 (1954). Mommaerts, W. F . Η. M. Am. J. Physiol 182, 585 ( 1955). Szent-Györgyi, A. Biol. Bull. 96, 140 ( 1 9 4 9 ) . Weber, Η. , and Portzehl, H. Progr. in Biophys. and Biophys. Chem. 4, 60 (1954). , and Ulbrecht, M. Biochim. et Biophys. Acta 11, 138 (1953); 13, 319 ( 1 9 5 4 ) . Schick, A. , and Hass, G. M. Science 109, 487 ( 1949). Perry, S. V. Biochem. J. 48, 257 ( 1951 ) .

6 residues per turn. As the photograph (Fig. 4 ) shows, the side chains bristle out from the helix core. With the 52 BARBARA W . LOW exception of prolyl and hydroxy-prolyl side chains (these are imino acid residues and do not have a free NH group to par­ ticipate in the helix hydrogen bond formation) the nature of the side-chain group does not stereochemically affect the forma­ tion of α-helical structure. A model of the α-helix structure FIG. 2. 5 A ) parallel to the axis [Reproduced by permission from Corey, R.

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